Identification and Expression Profiling of Two Saudi Arabia Catalase Genes from Wheat and Barley in Response to Abiotic and Hormonal Stresses (original) (raw)
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Plants
Catalase (CAT) is an antioxidant enzyme expressed by the CAT gene family and exists in almost all aerobic organisms. In fact, the CAT enzyme modulates the hydrogen peroxide (H2O2) contents in cells by translating this toxic compound into water (H2O) and O2− to reduce reactive oxygen species (ROS) contents in cells. ROS are produced as a result of biotic and abiotic environmental stressors. To avoid ROS toxicity, plants are armed with different enzymatic and non-enzymatic systems to decompose ROS. Among the enzymatic system, CAT proteins are well studied. CAT not only controls growth and development in plants but is also involved in plant defense against different stresses. So far, the CAT gene family has not been reported in durum wheat (Triticum turgidum ssp. durum L.). Therefore, a genome-wide comprehensive analysis was conducted to classify the CAT genes in the durum wheat genome. Here, six TdCAT genes were identified. Based on phylogenetics, the TdCAT genes belong to three group...
Comprehensive Functional Analysis of the Catalase Gene Family in Arabidopsis thaliana
Journal of Integrative Plant Biology, 2008
In Arabidopsis, catalase (CAT) genes encode a small family of proteins including CAT1, CAT2 and CAT3, which catalyze the decomposition of hydrogen peroxide (H 2 O 2 ) and play an important role in controlling homeostasis of reactive oxygen species (ROS). Here, we analyze the expression profiles and activities of three catalases under different treatments including drought, cold, oxidative stresses, abscisic acid and salicylic acid in Arabidopsis. Our results reveal that CAT1 is an important player in the removal of H 2 O 2 generated under various environmental stresses. CAT2 and CAT3 are major H 2 O 2 scavengers that contribute to ROS homeostasis in light or darkness, respectively. In addition, CAT2 is activated by cold and drought stresses and CAT3 is mainly enhanced by abscisic acid and oxidative treatments as well as at the senescence stage. These results, together with previous data, suggest that the network of transcriptional control explains how CATs and other scavenger enzymes such as peroxidase and superoxide dismutase may be coordinately regulated during development, but differentially expressed in response to different stresses for controlling ROS homeostasis.
2019
Peroxidases (POXs) and Catalases (CATs) are the main antioxidant enzymes involved in scavenging H2O2 in living cells. Different POXs and CATs may be capable of exhibiting interaction with the constituents of the plant cell. Whereas the activity or gene expression of POXs and CATs has been investigated in potato plants, their interactions with other proteins in this crop have not been investigated till now. Determining Protein-Protein Interaction (PPI) networks could be important in providing crucial insights into the regulation of plant defense responses to biotic and abiotic stresses. STRING analysis revealed interaction of cationic, suberization-associated anionic, and Class III peroxidases in potato with several enzymes involved in lignin biosynthesis and phenylpropanoid pathways, which was in accordance with close phylogenetic relationship of the three potato peroxidases investigated in this study. The CAT1 enzyme in potato interacted with several enzymes involved in ROS product...
Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana
Gene, 2002
Higher plants possess a large set of the classical guaiacol peroxidases (class III peroxidases, E.C. 1.11.1.7). These enzymes have been implicated in a wide array of physiological processes such as H 2 O 2 detoxification, auxin catabolism and lignin biosynthesis and stress response (wounding, pathogen attack, etc.). During the last 10 years, molecular cloning has allowed the isolation and characterization of several genes encoding peroxidases in plants. The achievement of the large scale Arabidopsis genome sequencing, combined with the DNA complementary to RNA (cDNA) expressed sequence tags projects, provided the opportunity to draw up the first comprehensive list of peroxidases in a plant. By screening the available databases, we have identified 73 peroxidase genes throughout the Arabidopsis genome. The evolution of the peroxidase multigene family has been investigated by analyzing the gene structure (intron/exon) in correlation with the phylogenetic relationships between the isoperoxidases. An evolutionary pattern of extensive gene duplications can be inferred and is discussed. Using a cDNA array procedure, the expression pattern of 23 peroxidases was established in the different organs of the plant. All the tested peroxidases were expressed at various levels in roots, while several were also detected in stems, leaves and flowers. The specific functions of these genes remain to be determined. q
Computational analyses and annotations of the Arabidopsis peroxidase gene family
Febs Letters, 1998
Classical heme-containing plant peroxidases have been ascribed a wide variety of functional roles related to development, defense, lignification, and hormonal signaling. More than 40 peroxidase genes are now known in Arabidopsis thaliana for which functional association is complicated by a general lack of peroxidase substrate specificity. Computational analysis was performed on 30 near full-length Arabidopsis peroxidase cDNAs for annotation of start codons and signal peptide cleavage sites. A compositional analysis revealed that 23 of the 30 peroxidase cDNAs have 5P untranslated regions containing 40^71% adenine, a rare feature observed also in cDNAs which predominantly encode stress-induced proteins, and which may indicate translational regulation.
Computational analyses and annotations of theArabidopsisperoxidase gene family
FEBS Letters, 1998
Classical heme-containing plant peroxidases have been ascribed a wide variety of functional roles related to development, defense, lignification, and hormonal signaling. More than 40 peroxidase genes are now known in Arabidopsis thaliana for which functional association is complicated by a general lack of peroxidase substrate specificity. Computational analysis was performed on 30 near full-length Arabidopsis peroxidase cDNAs for annotation of start codons and signal peptide cleavage sites. A compositional analysis revealed that 23 of the 30 peroxidase cDNAs have 5P untranslated regions containing 40^71% adenine, a rare feature observed also in cDNAs which predominantly encode stress-induced proteins, and which may indicate translational regulation.
Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana
European Journal of Biochemistry, 2002
Understanding peroxidase function in plants is complicated by the lack of substrate specificity, the high number of genes, their diversity in structure and our limited knowledge of peroxidase gene transcription and translation. In the present study we sequenced expressed sequence tags (ESTs) encoding novel heme-containing class III peroxidases from Arabidopsis thaliana and annotated 73 full-length genes identified in the genome. In total, transcripts of 58 of these genes have now been observed. The expression of individual peroxidase genes was assessed in organ-specific EST libraries and compared to the expression of 33 peroxidase genes which we analyzed in whole plants 3, 6, 15, 35 and 59 days after sowing. Expression was assessed in root, rosette leaf, stem, cauline leaf, flower bud and cell culture tissues using the gene-specific and highly sensitive reverse transcriptasepolymerase chain reaction (RT-PCR).We predicted that 71 genes could yield stable proteins folded similarly to horseradish peroxidase (HRP). The putative mature peroxidases derived from these genes showed 28-94% amino acid sequence identity and were all targeted to the endoplasmic reticulum by N-terminal signal peptides. In 20 peroxidases these signal peptides were followed by various N-terminal extensions of unknown function which are not present in HRP. Ten peroxidases showed a C-terminal extension indicating vacuolar targeting. We found that the majority of peroxidase genes were expressed in root. In total, class III peroxidases accounted for an impressive 2.2% of root ESTs. Rather few peroxidases showed organ specificity. Most importantly, genes expressed constitutively in all organs and genes with a preference for root represented structurally diverse peroxidases (< 70% sequence identity). Furthermore, genes appearing in tandem showed distinct expression profiles. The alignment of 73 Arabidopsis peroxidase sequences provides an easy access to the identification of orthologous peroxidases in other plant species and will provide a common platform for combining knowledge of peroxidase structure and function relationships obtained in various species.
Catalase is encoded by a multigene family in Arabidopsis thaliana (L.) Heynh
Plant …, 1996
The catalase multigene family in Arabidopsis includes three genes encoding individual subunits that associate to form at least six isozymes that are readily resolved by nondenaturing gel electrophoresis. CATl and CAT3map to chromosome 1 , and CAT2maps to chromosome 4. The nucleotide sequences of the three coding regions are 70 to 72% identical. The amino acid sequences of the three catalase subunits are 75 to 84% identical and 87 to 94% similar, considering conservative substitutions. Both the individual isozymes and the individual subunit mRNAs show distinct patterns of spatial (organ-specific) expression. Six isozymes are detected in flowers and leaves and two are seen in roots. Similarly, mRNA abundance of the three genes varies among organs. All three mRNAs are highly expressed in bolts, and CAT2 and CAT3 are highly expressed in leaves. Catalase (H,O,:H,O, oxidoreductase; EC 1.11.1.6) is a tetrameric iron porphyrin protein that catalyzes the dismutation of H,O, to water and oxygen. First characterized in 1901 (Loew, 1901), catalase was one of the earliest enzymes to be isolated in a state of high purity (Sumner and Dounce, 1937). No multicellular organism has been found that does not possess at least some catalase activity (Scandalios, 1987). Peroxisomes, for which catalase activity is a biochemical marker, are present in almost a11 eukaryotes (Subramani, 1993). Catalases, together with superoxide dismutases and hydroperoxidases, make up a defense system for the scavenging of superoxide radicals and hydroperoxides (Beyer and Fridovich, 1987). In addition to the active oxygen present in most cells as a by-product of mitochondrial electron transport and the P-oxidation of fatty acids,
Catalase and ascorbate peroxidase-representative H2O2-detoxifying heme enzymes in plants
Environmental science and pollution research international, 2016
Plants have to counteract unavoidable stress-caused anomalies such as oxidative stress to sustain their lives and serve heterotrophic organisms including humans. Among major enzymatic antioxidants, catalase (CAT; EC 1.11.1.6) and ascorbate peroxidase (APX; EC 1.11.1.11) are representative heme enzymes meant for metabolizing stress-provoked reactive oxygen species (ROS; such as H2O2) and controlling their potential impacts on cellular metabolism and functions. CAT mainly occurs in peroxisomes and catalyzes the dismutation reaction without requiring any reductant; whereas, APX has a higher affinity for H2O2 and utilizes ascorbate (AsA) as specific electron donor for the reduction of H2O2 into H2O in organelles including chloroplasts, cytosol, mitochondria, and peroxisomes. Literature is extensive on the glutathione-associated H2O2-metabolizing systems in plants. However, discussion is meager or scattered in the literature available on the biochemical and genomic characterization as we...